ECP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ECP_HUMAN
• UniProt AC: P12724
• Protein Name: Eosinophil cationic protein
• Gene Name: RNASE3
• Organism: Homo sapiens (Human).
• Sequence Length: 160
• Subcellular Localization: Secreted. Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus.
• Protein Description: Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content..
• Protein Sequence: MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTI

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Nitrated tyrosine	AMRAINNYRWRCKNQ EEHHHHHCEEEECCC	13.68	-
60	Nitration	AMRAINNYRWRCKNQ EEHHHHHCEEEECCC	13.68	18694936
60	Nitration	AMRAINNYRWRCKNQ EEHHHHHCEEEECCC	13.68	18694936
84	N-linked_Glycosylation	NVVNVCGNQSIRCPH HHEHHCCCCCEECCC	27.57	UniProtKB CARBOHYD
92	N-linked_Glycosylation	QSIRCPHNRTLNNCH CCEECCCCCCCCCCC	24.63	UniProtKB CARBOHYD
119	N-linked_Glycosylation	LINPGAQNISNCTYA ECCCCCCCCCCCEEC	38.84	UniProtKB CARBOHYD
134	Phosphorylation	DRPGRRFYVVACDNR CCCCCEEEEEEECCC	7.69	22817900
149	Phosphorylation	DPRDSPRYPVVPVHL CCCCCCCCCCCCEEE	12.08	24719451
158	Phosphorylation	VVPVHLDTTI----- CCCEEEECCC-----	32.52	24719451
159	Phosphorylation	VPVHLDTTI------ CCEEEECCC------	25.10	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ECP_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ECP_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ECP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POTEI_HUMAN	POTEI	physical	28514442
RINI_HUMAN	RNH1	physical	28514442
GTPB2_HUMAN	GTPBP2	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
BLK_HUMAN	BLK	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
GNAZ_HUMAN	GNAZ	physical	28514442
GGPPS_HUMAN	GGPS1	physical	28514442
UBAC1_HUMAN	UBAC1	physical	28514442
EFR3B_HUMAN	EFR3B	physical	28514442
RN123_HUMAN	RNF123	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Nitration

"Post-translational tyrosine nitration of eosinophil granule toxinsmediated by eosinophil peroxidase.";
Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N.,Acharya K.R., Schmid-Grendelmeier P., Simon H.-U., Schwarz H.,Tsutsui M., Shimokawa H., Bellon G., Lee J.J., Przybylski M.,Doering G.;
J. Biol. Chem. 283:28629-28640(2008).
Cited for: NITRATION AT TYR-60.
PubMed: 18694936